The ubiquitin ligase RNF181 stabilizes ERα and modulates breast cancer progression
Open accessAbstract
ERα positive breast cancer accounts for 70% of breast malignancies. Compared with ERα negative types, ERα positive breast cancer could be effective controlled by endocrine therapy. However, more than half of the patients will develop endocrine resistance, making it an important clinical issue for breast cancer therapy. Endocrine resistance might be caused by multiple alternations, including the components of ERα signaling, during tumor progression. Thus, it is urgent and necessary to uncover the molecular mechanisms that controls ERα expression and stability to improve breast cancer therapeutics. In our current study, we identifies that the ubiquitin ligase RNF181 stabilizes ERα and facilitates breast cancer progression. The expression of RNF181 is correlated with ERα level in human breast tumors and relates to poor survival in endocrine-treated patients. RNF181 depletion inhibits breast cancer progression in vivo and in vitro, reduces ERα protein level and its target gene expression, such as PS2 and GREB1. Unbiased RNA sequencing analysis indicates RNF181 is necessary for ERα signature gene expression in whole genomic level. Immuno-precipitation assays indicate that RNF181 associates with ERα and promotes its stability possibly via inducing ERα K63-linked poly-ubiquitination. In conclusion, our data implicate a non-genomic mechanism by RNF181 via stabilizing ERα protein controls ERα target gene expression linked to breast cancer progression.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
TRIM56, RNF181, and RNF2 stabilize ERα expression.
“It has been reported that the ubiquitin ligases TRIM56, RNF181, and RNF2 stabilize ERα expression30–32.”
From Harnessing artificial intelligence to identify Bufalin as a molecular glue degrader of estrogen receptor alpha (2025) · cites this paper as [31]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Bray, F., Ferlay, J., Soerjomataram, I., Siegel, R. L., Torre, L. A., & Jemal, A. (2018) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.21492 · Cited by 84,109 · see citing works
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679 · see citing works
Sequence and Expression of Human Estrogen Receptor Complementary DNA
Greene, G. L., Gilna, P., Waterfield, M. D., BAKER, A. J., Hort, Y., & Shine, J. (1986) · Science · doi:10.1126/science.3753802 · Cited by 1,311 · see citing works
Biological determinants of endocrine resistance in breast cancer
Musgrove, E. A., & Sutherland, R. L. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2713 · Cited by 1,254 · see citing works
Onitilo, A. A., Engel, J. M., Greenlee, R. T., & Mukesh, B. N. (2009) · Clinical Medicine & Research · doi:10.3121/cmr.2009.825 · Cited by 1,023 · see citing works
Bunone, G., Briand, P.-A., Miksicek, R. J., & Picard, D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00571.x · Cited by 985 · see citing works
SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
Ikeda, F., Deribe, Y. L., Skånland, S. S., Stieglitz, B., Grabbe, C., Franz-Wachtel, M., van Wijk, S. J. L., Goswami, P., Nagy, V., Terzic, J., et al. (2011) · Nature · doi:10.1038/nature09814 · Cited by 745 · see citing works
HECT and RING finger families of E3 ubiquitin ligases at a glance
Metzger, M. B., Hristova, V. A., & Weissman, A. M. (2012) · Journal of Cell Science · doi:10.1242/jcs.091777 · Cited by 622 · see citing works
SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
Tokunaga, F., Nakagawa, T., Nakahara, M., Saeki, Y., Taniguchi, M., Sakata, S.-I., Tanaka, K., Nakano, H., & Iwai, K. (2011) · Nature · doi:10.1038/nature09815 · Cited by 609 · see citing works
p300 is a component of an estrogen receptor coactivator complex.
Hanstein, B., Eckner, R., DiRenzo, J., Halachmi, S., Liu, H., Searcy, B. T., Kurokawa, R., & Brown, M. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11540 · Cited by 396 · see citing works
Wang, C., Fu, M., Angeletti, R. H., Siconolfi-Baez, L., Reutens, A. T., Albanese, C., Lisanti, M. P., Katzenellenbogen, B. S., Kato, S., Hopp, T., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100800200 · Cited by 365 · see citing works
Estrogen Receptor Alpha in Human Breast Cancer: Occurrence and Significance
Ali, S., & Coombes, R. (2000) · Journal of mammary gland biology and neoplasia · doi:10.1023/a:1009594727358 · Cited by 336 · see citing works
Vaz-Luís, I., Ottesen, R. A., Hughes, M. E., Mamet, R., Burstein, H. J., Edge, S. B., Gonzalez-Angulo, A. M., Moy, B., Rugo, H. S., Theriault, R. L., et al. (2014) · Journal of Clinical Oncology · doi:10.1200/jco.2013.53.1608 · Cited by 245 · see citing works
Understanding the Global Cancer Statistics 2018: implications for cancer control
Cai, Z., & Liu, Q. (2019) · Science China Life Sciences · doi:10.1007/s11427-019-9816-1 · Cited by 150 · see citing works
Pathways to Endocrine Therapy Resistance in Breast Cancer
Haque, M., & Desai, K. V. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00573 · Cited by 135 · see citing works
Shaaban, A. M., Sloane, J. P., West, C. R., & Foster, C. S. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64879-1 · Cited by 126 · see citing works
Endocrine therapy resistance: new insights
Lei, J. T., Anurag, M., Haricharan, S., Gou, X., & Ellis, M. J. (2019) · The Breast · doi:10.1016/s0960-9776(19)31118-x · Cited by 120 · see citing works
The ring between ring fingers (RBR) protein family
Eisenhaber, B., Chumak, N., Eisenhaber, F., & Hauser, M. (2007) · Genome biology · doi:10.1186/gb-2007-8-3-209 · Cited by 119 · see citing works
Zhu, J., Zhao, C., Razavirad, A., Zhuang, T., Jonsson, P., Liang, N., Williams, C., Lin, C.-Y., Qiao, Y., Zendehdel, K., et al. (2014) · Oncogene · doi:10.1038/onc.2013.573 · Cited by 99 · see citing works
Self-citationRegulation of estrogen signaling and breast cancer proliferation by an ubiquitin ligase TRIM56
Xue, M., Zhang, K., Mu, K., Xu, J., Yang, H., Liu, Y., Wang, B., Wang, Z., Li, Z., Kong, Q., et al. (2019) · Oncogenesis · doi:10.1038/s41389-019-0139-x · Cited by 97 · see citing works
Self-citationRenaud, J., Bischoff, S. F., Buhl, T., Floersheim, P., Fournier, B., Halleux, C. M., Kallen, J. A., Keller, H., Schlaeppi, J.-M., & Stark, W. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm030086h · Cited by 89 · see citing works
Renaud, J., Bischoff, S. F., Buhl, T., Floersheim, P., Fournier, B., Geiser, M., Halleux, C. M., Kallen, J. A., Keller, H., & Ramage, P. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm040858p · Cited by 67 · see citing works
SMURF1 facilitates estrogen receptor ɑ signaling in breast cancer cells
Yang, H., Yu, N. H., Xu, J., Ding, X., Deng, W., Wu, G., Li, X., Hou, Y., Liu, Z., Zhao, Y., et al. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0672-z · Cited by 61 · see citing works
Self-citationNew insights into acquired endocrine resistance of breast cancer
Fan, P., & Jordan, V. C. (2019) · Cancer Drug Resistance · doi:10.20517/cdr.2019.13 · Cited by 56 · see citing works
Jin, H., Cheng, X. J., Pei, Y., Fu, J., Lyu, Z., Peng, H., Yao, Q., Jiang, Y., Luo, L., & Zhuo, H. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.12.012 · Cited by 52 · see citing works
RNF8 identified as a co-activator of estrogen receptor α promotes cell growth in breast cancer
Wang, S., Luo, H., Wang, C., Sun, H., Sun, G., Sun, N., Zeng, K., Song, H., Zou, R., Zhou, T., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.02.011 · Cited by 50 · see citing works
SHARPIN Facilitates p53 Degradation in Breast Cancer Cells
Yang, H., Yu, S., Wang, W., Li, X., Hou, Y., Liu, Z., Shi, Y., Mu, K., Niu, G., Xu, J., et al. (2017) · Neoplasia · doi:10.1016/j.neo.2016.12.002 · Cited by 44 · see citing works
Self-citationNon-canonical Estrogen Signaling in Endocrine Resistance
Ranganathan, P., Nadig, N., & Nambiar, S. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00708 · Cited by 39 · see citing works
Negative Regulation of CARD11 Signaling and Lymphoma Cell Survival by the E3 Ubiquitin Ligase RNF181
Pedersen, S. M., Chan, W., Jattani, R. P., Mackie, D. S., & Pomerantz, J. L. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00876-15 · Cited by 37 · see citing works
SHARPIN stabilizes estrogen receptor α and promotes breast cancer cell proliferation
Zhuang, T., Yu, S., Zhang, L., Yang, H., Li, X., Hou, Y., Liu, Z., Shi, Y., Wang, W., Yu, N. H., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20368 · Cited by 35 · see citing works
Self-citationRN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin αIIbβ3
Brophy, T. M., Raab, M., Daxecker, H., Culligan, K., Lehmann, I. T., Chubb, A. J., Treumann, A., & Moran, N. M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.02.142 · Cited by 33 · see citing works
Protein interactions with the platelet integrin αIIb regulatory motif
Raab, M., Daxecker, H., Edwards, R. J., Treumann, A., Murphy, D. B., & Moran, N. M. (2010) · PROTEOMICS · doi:10.1002/pmic.200900621 · Cited by 18 · see citing works
RNF 168 facilitates oestrogen receptor ɑ transcription and drives breast cancer proliferation
Liu, Z., Zhang, J., Xu, J., Yang, H., Li, X., Hou, Y., Zhao, Y., Xue, M., Wang, B., Yu, N. H., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13694 · Cited by 15 · see citing works
Self-citationAbdel‐Magid, A. F. (2017) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00424 · Cited by 12 · see citing works
Overcoming endocrine resistance in neoadjuvant endocrine therapy for early breast cancer
Jackisch, C. (2019) · The Lancet Oncology · doi:10.1016/s1470-2045(19)30500-5 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Endocytosis in cancer and cancer therapy
Banushi, B., Joseph, S. R., Lum, B., Lee, J. J., & Simpson, F. (2023) · Nature reviews. Cancer · doi:10.1038/s41568-023-00574-6 · Cited by 245 · see citing works
Role of K63-linked ubiquitination in cancer
Cao, L., Liu, X., Zheng, B., Xing, C., & Liu, J. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01204-0 · Cited by 73 · see citing works
Mao, M., Chen, Y., Yang, J., Cheng, Y., Xu, L., Ji, F., Zhou, J., Zhang, X., Li, Z., Chen, C., et al. (2022) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2022-005668 · Cited by 51 · see citing works
cIAP1-based degraders induce degradation via branched ubiquitin architectures
Akizuki, Y., Morita, M., Mori, Y., Kaiho-Soma, A., Dixit, S., Endo, A., Shimogawa, M., Hayashi, G., Naito, M., Okamoto, A., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01178-1 · Cited by 44 · see citing works
Matteo, G., Leingartner, K., Rowan‐Carroll, A., Meier, M. J., Williams, A., Beal, M. A., Gagné, M., Farmahin, R., Wickramasuriya, S., Reardon, A. J. F., et al. (2022) · Toxicological Sciences · doi:10.1093/toxsci/kfac127 · Cited by 44 · see citing works
Yang, P., Xiao, Y., Wang, D., Yang, H., Li, Z., Zhang, C., Zhang, S., Zhu, J., Li, X., Su, P., et al. (2023) · Oncogene · doi:10.1038/s41388-023-02905-1 · Cited by 37 · see citing works
Self-citationMao, M., Jia, Y., Chen, Y., Yang, J., Xu, L., Zhang, X., Zhou, J., Li, Z., Chen, C., Ju, S., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04833-6 · Cited by 34 · see citing works
circRNA-SFMBT2 orchestrates ERα activation to drive tamoxifen resistance in breast cancer cells
Li, Z., Li, Y., Han, D., Wang, X., Li, C., Chen, T., Li, W., Liang, Y., Luo, D., Chen, B., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06006-5 · Cited by 33 · see citing works
Yang, H., Xue, M., Su, P., Zhou, Y., Li, X., Li, Z., Xia, Y., Zhang, C., Fu, M., Zheng, X., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02576-y · Cited by 28 · see citing works
Self-citationJiang, S., Liu, K., Jiang, T., Li, H., Wei, X., Wan, X., Zhong, C., Gong, R., Chen, Z., Zou, C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62288-7 · Cited by 23 · see citing works
Zhuang, T., Zhang, S., Liu, D., Li, Z., Li, X., Li, J., Yang, P., Zhang, C., Cui, J., Fu, M., et al. (2024) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-024-03160-2 · Cited by 17 · see citing works
Self-citationRegulation of P53 signaling in breast cancer by the E3 ubiquitin ligase RNF187
Li, X., Niu, Z., Sun, C., Zhuo, S., Yang, H., Yang, X. F., Liu, Y., Yan, C., Li, Z., Cao, Q., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04604-3 · Cited by 16 · see citing works
Self-citationRBCK1 is an endogenous inhibitor for triple negative breast cancer via hippo/YAP axis
Li, Z., Su, P., Ding, Y., Gao, H., Yang, H., Li, X., Yang, X., Xia, Y., Zhang, C., Fu, M., et al. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00963-8 · Cited by 16 · see citing works
Self-citationSaha, T., & Lukong, K. E. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1513225 · Cited by 19 · see citing works
Tecalco-Cruz, Á. C., Macías‐Silva, M., Ramírez‐Jarquín, J. O., & Ramírez-Jarquín, U. N. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.867448 · Cited by 11 · see citing works
Inhibition of RNF182 mediated by Bap promotes non-small cell lung cancer progression
Liu, Y., Ouyang, L., Mao, C., Chen, Y., Liu, N., Chen, L., Shi, Y., Xiao, D., Liu, S., & Tao, Y. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2022.1009508 · Cited by 11 · see citing works
The ubiquitin ligase RNF2 stabilizes ERα and modulates breast cancer progression
Yuan, L., Li, X., Yang, H., & Li, H. (2022) · Human Cell · doi:10.1007/s13577-022-00810-5 · Cited by 9 · see citing works
Self-citationEmerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis
Yin, X., Liu, Q., Liu, F., Tian, X., Yan, T., Han, J., & Jiang, S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.944460 · Cited by 8 · see citing works
UHRF1 modulates breast cancer cell growth via estrogen signaling
Luo, G., Li, Q., Yu, M., Wang, T., Zang, Y., Liu, Z., Niu, Z., Yang, H., & Lai, J. (2022) · Medical Oncology · doi:10.1007/s12032-022-01720-0 · Cited by 8 · see citing works
Self-citationDang, R., Qu, B., Guo, K., Zhou, S., Sun, H., Wang, W., Han, J., Feng, K., Lin, J., & Hu, Y. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2021.818813 · Cited by 6 · see citing works
Choi, S., & Paek, E. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100743 · Cited by 5 · see citing works
Xu, Y., Qian, T., Pan, H., Gu, Y., Xu, M., Bai, C., & Chen, W. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147773 · Cited by 4 · see citing works
Li, H., Liu, Y., Cai, Z., Li, K., Gao, S., Lan, A., Shu, D., He, K., Liu, X., Peng, Y., et al. (2025) · Advanced Science · doi:10.1002/advs.202509769 · Cited by 3 · see citing works
Li, Y., Xiang, Z.-Y., Xiong, J., Hou, Z.-W., Zhu, Z., & Bao, W.-W. (2021) · Acta Histochemica · doi:10.1016/j.acthis.2021.151733 · Cited by 2 · see citing works
Targeting FAM134B-DDX3X axis inhibiting AKT signaling in hepatocellular carcinoma
Mo, J., Chen, S., Liu, Q., Li, P., Xu, L., Long, X., Liang, H., Zhang, B., & Chen, J. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08080-3 · Cited by 1 · see citing works
MicroRNA-375 promotes tamoxifen resistance by stabilizing ERα via UBE3A-mediated ubiquitination
Xue, D., Xie, Y., Sun, J., Li, J., Huang, Y., Yang, Y., Liang, L., Li, Q., Mu, G., Meng, Q., et al. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116434 · Cited by 1 · see citing works
Tecalco-Cruz, Á. C., Ramírez‐Jarquín, J. O., Macías‐Silva, M., Sosa‐Garrocho, M., & López‐Camarillo, C. (2022) · Exon Publications eBooks · doi:10.36255/exon-publications-breast-cancer-protacs
Cui, H., Zhou, X., Chen, S., Liu, X., Song, H., Gan, L., Wu, Z., Liao, Y., Liao, Y., & Zhong, L. (2024) · Research Square · doi:10.21203/rs.3.rs-3896180/v1
Ling, C., Cao, N., Wang, H., Wan, Y., Liang, X., Guo, J., Xiao, M., Zhang, Q., & Zhai, Z. (2025) · International Journal of General Medicine · doi:10.2147/ijgm.s502644
Yang, H., Xue, M., Su, P., Zhou, Y., Li, X., Li, Z., Xia, Y., Zhang, C., Fu, M., Zheng, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22606181
Self-citationYang, H., Xue, M., Su, P., Zhou, Y., Li, X., Li, Z., Xia, Y., Zhang, C., Fu, M., Zheng, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22606184
Self-citationYang, H., Xue, M., Su, P., Zhou, Y., Li, X., Li, Z., Xia, Y., Zhang, C., Fu, M., Zheng, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22606193
Self-citationYang, H., Xue, M., Su, P., Zhou, Y., Li, X., Li, Z., Xia, Y., Zhang, C., Fu, M., Zheng, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22606187
Self-citationZhuang, T., Zhang, S., Liu, D., Li, Z., Li, X., Li, J., Yang, P., Zhang, C., Cui, J., Fu, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26944512
Self-citationYang, H., Xue, M., Su, P., Zhou, Y., Li, X., Li, Z., Xia, Y., Zhang, C., Fu, M., Zheng, X., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22606190
Self-citationZhuang, T., Zhang, S., Liu, D., Li, Z., Li, X., Li, J., Yang, P., Zhang, C., Cui, J., Fu, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26944509
Self-citationXia, J., Fei, S., Luo, W., Zhou, M., Kong, Y., Huang, Y., Swevers, L., & Feng, M. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1013848
Zeng, K., Wang, A.-Q., Sun, H.-M., Wang, C.-Y., Wang, S.-L., Zou, R.-L., Yang, D.-J., Bai, Y., Wang, M.-L., Xu, Y.-Y., et al. (2026) · npj Precision Oncology · doi:10.1038/s41698-026-01568-x
Liu, J., Peng, Y., Ming, Y., Chen, M., Muhammad, I., Qi, Y., Wang, L., Huang, G., & Wei, G. (2026) · Journal of Invertebrate Pathology · doi:10.1016/j.jip.2026.108705
- Authors
- Zhu, J., Li, X., Su, P., Xue, M., Zang, Y., & Ding, Y.
- Affiliations
- Shandong University (CN)
- Henan Medical University (CN)
- Corresponding author
- Zhu, Jian
- Ding, Yinlu
- Venue
- Oncogene
- Published
- 2020-09-24
- Volume
- 39
- Issue
- 44
- Pages
- 6776-6788
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- PMC
- PMC7605433
- OpenAlex
- W3089312151
- Cited by
- 39
- References
- 35
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 5 · 2023: 9 · 2022: 14 · 2021: 1
- FWCI
- 3.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Oncogene (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Shandong University
- National Natural Science Foundation of China
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Breast Cancer Treatment Studies
- Keywords
- estrogen receptor alpha, protein stability, ubiquitin ligase, breast cancer progression, endocrine therapy resistance, K63-linked ubiquitination, pS2, GREB1, endocrine therapy
- MeSH terms
- Protein Domains, Progression-Free Survival, Animals, Breast, Breast Neoplasms, Female, Humans, Signal Transduction, Gene Expression Regulation, Neoplastic, Sequence Analysis, RNA, Disease Progression, Antineoplastic Agents, Hormonal, Drug Resistance, Neoplasm, Gene Expression Profiling, Xenograft Model Antitumor Assays, Ubiquitin-Protein Ligases, Estrogen Receptor alpha, Mice, Ubiquitination, Protein Stability, Gene Knockdown Techniques, HEK293 Cells, MCF-7 Cells, Datasets as Topic
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review